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Vitaly Kushnirov

Research Profile

Chemicals & Drugs

Living Beings

Genes & Molecular Sequences

Physiology

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Molecular Sequence Data

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Prion Diseases

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Publications

TOP 3
Olga V Mitkevich; Elizaveta R Surina; Sergei V Benevolensky; Natalia V Kochneva-Pervukhova; Vitaly V Kushnirov; Michael D Ter-Avanesyan
DNA aptamers detecting generic amyloid epitopes.
Alexander I Alexandrov; Alla B Polyanskaya; Genrikh V Serpionov; Michael D Ter-Avanesyan; Vitaly V Kushnirov
The effects of amino acid composition of glutamine-rich domains on amyloid formation and fragmentation.
E G Afanasieva; Vitaly V Kushnirov; Michael D Ter-Avanesyan
Interspecies transmission of prions.

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All Publications

2012: Olga V Mitkevich; Elizaveta R Surina; Sergei V Benevolensky; Natalia V Kochneva-Pervukhova; Vitaly V Kushnirov; Michael D Ter-Avanesyan
DNA aptamers detecting generic amyloid epitopes.
Prion 2012;6(4):400-6.
2012: Alexander I Alexandrov; Alla B Polyanskaya; Genrikh V Serpionov; Michael D Ter-Avanesyan; Vitaly V Kushnirov
The effects of amino acid composition of glutamine-rich domains on amyloid formation and fragmentation.
PloS one 2012;7(10):e46458.
2011: E G Afanasieva; Vitaly V Kushnirov; Michael D Ter-Avanesyan
Interspecies transmission of prions.
Biochemistry. Biokhimii͡a 2011;76(13):1375-84.
2011: Evgenia G Afanasieva; Vitaly V Kushnirov; Mick F Tuite; Michael D Ter-Avanesyan
Molecular basis for transmission barrier and interference between closely related prion proteins in yeast.
The Journal of biological chemistry 2011;286(18):15773-80.
2010: Valery N Urakov; Aleksandra B Vishnevskaya; Ilya M Alexandrov; Vitaly V Kushnirov; Vladimir N Smirnov; Michael D Ter-Avanesyan
Interdependence of amyloid formation in yeast: implications for polyglutamine disorders and biological functions.
Prion 2010;4(1):45-52.
2008: Ilya M Alexandrov; Aleksandra B Vishnevskaya; Michael D Ter-Avanesyan; Vitaly V Kushnirov
Appearance and propagation of polyglutamine-based amyloids in yeast: tyrosine residues enable polymer fragmentation.
The Journal of biological chemistry 2008;283(22):15185-92.
2007: Vitaly V Kushnirov; Aleksandra B Vishnevskaya; Ilya M Alexandrov; Michael D Ter-Avanesyan
Prion and nonprion amyloids: a comparison inspired by the yeast Sup35 protein.
Prion 2007;1(3):179-84.
2007: A B Vishnevskaia; Vitaly V Kushnirov; MD Ter-Avanesian
[Neurodegenerative amyloidoses: the yeast model].
Molekuliarnaia biologiia 2007;41(2):346-54.
2006: Vitaly V Kushnirov; Ilya M Alexandrov; Olga V Mitkevich; Irina S Shkundina; Michael D Ter-Avanesyan
Purification and analysis of prion and amyloid aggregates.
Methods (San Diego, Calif.) 2006;39(1):50-5.
2006: Irina S Shkundina; Vitaly V Kushnirov; Mick F Tuite; Michael D Ter-Avanesyan
The role of the N-terminal oligopeptide repeats of the yeast Sup35 prion protein in propagation and transmission of prion variants.
Genetics 2006;172(2):827-35.
2006: Sviatoslav Bagriantsev; Vitaly V Kushnirov; Susan Liebman
Analysis of amyloid aggregates using agarose gel electrophoresis.
Methods in enzymology 2006;412():33-48.
2005: Aleksandra B Salnikova; Dmitry Kryndushkin; Vladimir N Smirnov; Vitaly V Kushnirov; Michael D Ter-Avanesyan
Nonsense suppression in yeast cells overproducing Sup35 (eRF3) is caused by its non-heritable amyloids.
The Journal of biological chemistry 2005;280(10):8808-12.
2004: Dmitry Kryndushkin; I M Aleksandrov; Vitaly V Kushnirov; MD Ter-Avanesian
[Yeast as a model for studying the prion and amyloid occurrence].
Rossiĭskii fiziologicheskiĭ zhurnal imeni I.M. Sechenova / Rossiĭskaia akademiia nauk 2004;90(5):645-57.
2003: Dmitry Kryndushkin; Ilya M Alexandrov; Michael D Ter-Avanesyan; Vitaly V Kushnirov
Yeast [PSI+] prion aggregates are formed by small Sup35 polymers fragmented by Hsp104.
The Journal of biological chemistry 2003;278(49):49636-43.
2002: Igor A Valouev; Vitaly V Kushnirov; Michael D Ter-Avanesyan
Yeast polypeptide chain release factors eRF1 and eRF3 are involved in cytoskeleton organization and cell cycle regulation.
Cell motility and the cytoskeleton 2002;52(3):161-73.
2002: Dmitry Kryndushkin; Vladimir N Smirnov; Michael D Ter-Avanesyan; Vitaly V Kushnirov
Increased expression of Hsp40 chaperones, transcriptional factors, and ribosomal protein Rpp0 can cure yeast prions.
The Journal of biological chemistry 2002;277(26):23702-8.
2001: Agnieszka Chacinska; B Szczesniak; Natalia V Kochneva-Pervukhova; Vitaly V Kushnirov; Michael D Ter-Avanesyan; Magdalena Boguta
Ssb1 chaperone is a [PSI+] prion-curing factor.
Current genetics 2001;39(2):62-7.
2001: Natalia V Kochneva-Pervukhova; Maria B Chechenova; Igor A Valouev; Vitaly V Kushnirov; Vladimir N Smirnov; Michael D Ter-Avanesyan
[Psi(+)] prion generation in yeast: characterization of the 'strain' difference.
Yeast (Chichester, England) 2001;18(6):489-97.
2001: Valery N Urakov; Igor A Valouev; E I Lewitin; Sergey Paushkin; V S Kosorukov; Vitaly V Kushnirov; Vladimir N Smirnov; Michael D Ter-Avanesyan
Itt1p, a novel protein inhibiting translation termination in Saccharomyces cerevisiae.
BMC molecular biology 2001;2():9.
2000: Vitaly V Kushnirov; Dmitry Kryndushkin; Magdalena Boguta; Vladimir N Smirnov; Michael D Ter-Avanesyan
Chaperones that cure yeast artificial [PSI+] and their prion-specific effects.
Current biology : CB 2000;10(22):1443-6.
2000: Vitaly V Kushnirov
Rapid and reliable protein extraction from yeast.
Yeast (Chichester, England) 2000;16(9):857-60.
2000: Vitaly V Kushnirov; Natalia V Kochneva-Pervukhova; Maria B Chechenova; N S Frolova; Michael D Ter-Avanesyan
Prion properties of the Sup35 protein of yeast Pichia methanolica.
The EMBO journal 2000;19(3):324-31.
1999: Michael D Ter-Avanesyan; Vitaly V Kushnirov
Prions: infectious proteins with genetic properties.
Biochemistry. Biokhimii͡a 1999;64(12):1382-90.
1998: Natalia V Kochneva-Pervukhova; Sergey Paushkin; Vitaly V Kushnirov; Brian S Cox; Mick F Tuite; Michael D Ter-Avanesyan
Mechanism of inhibition of Psi+ prion determinant propagation by a mutation of the N-terminus of the yeast Sup35 protein.
The EMBO journal 1998;17(19):5805-10.
1998: Vitaly V Kushnirov; Michael D Ter-Avanesyan
Structure and replication of yeast prions.
Cell 1998;94(1):13-6.
1998: MD Ter-Avanesian; Sergey Paushkin; Vitaly V Kushnirov; Natalia V Kochneva-Pervukhova
[Molecular mechanisms of "protein heredity": yeast prions].
Molekuliarnaia biologiia 1998;32(1):32-42.
1997: Sergey Paushkin; Vitaly V Kushnirov; Vladimir N Smirnov; Michael D Ter-Avanesyan
In vitro propagation of the prion-like state of yeast Sup35 protein.
Science (New York, N.Y.) 1997;277(5324):381-3.
1997: A R Dagkesamanskaia; Vitaly V Kushnirov; Sergey Paushkin; MD Ter-Avanesian
[Fusion of glutathione S-transferase with the N-terminus of yeast Sup35p protein inhibits its prion-like properties].
Genetika 1997;33(5):610-5.
1997: I Stansfield; Vitaly V Kushnirov; K M Jones; Mick F Tuite
A conditional-lethal translation termination defect in a sup45 mutant of the yeast Saccharomyces cerevisiae.
European journal of biochemistry / FEBS 1997;245(3):557-63.
1997: Sergey Paushkin; Vitaly V Kushnirov; Vladimir N Smirnov; Michael D Ter-Avanesyan
Interaction between yeast Sup45p (eRF1) and Sup35p (eRF3) polypeptide chain release factors: implications for prion-dependent regulation.
Molecular and cellular biology 1997;17(5):2798-805.
1996: Irina Derkatch; Yury O Chernoff; Vitaly V Kushnirov; S G Inge-Vechtomov; Susan Liebman
Genesis and variability of [PSI] prion factors in Saccharomyces cerevisiae.
Genetics 1996;144(4):1375-86.
1996: Sergey Paushkin; Vitaly V Kushnirov; Vladimir N Smirnov; Michael D Ter-Avanesyan
Propagation of the yeast prion-like [psi+] determinant is mediated by oligomerization of the SUP35-encoded polypeptide chain release factor.
The EMBO journal 1996;15(12):3127-34.
1995: I Stansfield; K M Jones; Vitaly V Kushnirov; A R Dagkesamanskaya; A I Poznyakovski; Sergey Paushkin; C R Nierras; Brian S Cox; Michael D Ter-Avanesyan; Mick F Tuite
The products of the SUP45 (eRF1) and SUP35 genes interact to mediate translation termination in Saccharomyces cerevisiae.
The EMBO journal 1995;14(17):4365-73.
1995: Vitaly V Kushnirov; MD Ter-Avanesian; Vladimir N Smirnov
[Structure and functional similarity of yeast Sup35p and Ure2p proteins to mammalian prions].
Molekuliarnaia biologiia 1995;29(4):750-5.
1994: Michael D Ter-Avanesyan; A R Dagkesamanskaya; Vitaly V Kushnirov; Vladimir N Smirnov
The SUP35 omnipotent suppressor gene is involved in the maintenance of the non-Mendelian determinant [psi+] in the yeast Saccharomyces cerevisiae.
Genetics 1994;137(3):671-6.
1993: Michael D Ter-Avanesyan; Vitaly V Kushnirov; A R Dagkesamanskaya; S A Didichenko; Yury O Chernoff; S G Inge-Vechtomov; Vladimir N Smirnov
Deletion analysis of the SUP35 gene of the yeast Saccharomyces cerevisiae reveals two non-overlapping functional regions in the encoded protein.
Molecular microbiology 1993;7(5):683-92.
1990: Vitaly V Kushnirov; Michael D Ter-Avanesyan; S A Didichenko; Vladimir N Smirnov; Yury O Chernoff; Irina Derkatch; O N Novikova; S G Inge-Vechtomov; M A Neistat; Ilya Tolstorukov
Divergence and conservation of SUP2 (SUP35) gene of yeast Pichia pinus and Saccharomyces cerevisiae.
Yeast (Chichester, England) 1990;6(6):461-72.
1990: Vitaly V Kushnirov; MD Ter-Avanesian; A R Dagkesamanskaia; Iu O Chernov; S G Inge-Vechtomov; Vladimir N Smirnov
[Deletion analysis of the SUP2 gene in Saccharomyces cerevisiae].
Molekuliarnaia biologiia 1990;24(4):1037-41.
1990: Vitaly V Kushnirov; MD Ter-Avanesian; Vladimir N Smirnov; Iu O Chernov; Irina Derkatch; O N Novikova; S G Inge-Vechtomov; M A Neĭstat; Ilya Tolstorukov
[Comparative analysis of the structure of SUP2 genes in Pichia pinus and Saccharomyces cerevisiae].
Molekuliarnaia biologiia 1990;24(4):1024-36.
1988: Vitaly V Kushnirov; Michael D Ter-Avanesyan; M V Telckov; A P Surguchov; Vladimir N Smirnov; S G Inge-Vechtomov
Nucleotide sequence of the SUP2 (SUP35) gene of Saccharomyces cerevisiae.
Gene 1988;66(1):45-54.
1987: Vitaly V Kushnirov; Michael D Ter-Avanesyan; A P Surguchov; Vladimir N Smirnov; S G Inge-Vechtomov
Localization of possible functional domains in sup2 gene product of the yeast Saccharomyces cerevisiae.
FEBS letters 1987;215(2):257-60.